Identification of a major determinant for serine-threonine kinase phosphoacceptor specificity.
Catherine Chen,Byung Hak Ha,Anastasia F. Thévenin,Hua Jane Lou,Rong Zhang,Kevin Y. Yip,Kevin Y. Yip,Jeffrey R. Peterson,Mark Gerstein,Philip M. Kim,Panagis Filippakopoulos,Panagis Filippakopoulos,Stefan Knapp,Titus J. Boggon,Benjamin E. Turk +14 more
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TLDR
It is shown that a residue located in the kinase activation segment, which is termed the “DFG+1” residue, acts as a major determinant for serine-threonine phosphorylation site specificity.About:
This article is published in Molecular Cell.The article was published on 2014-01-09 and is currently open access. It has received 96 citations till now. The article focuses on the topics: Serine/threonine-specific protein kinase & Protein-Serine-Threonine Kinases.read more
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mTORC1 Phosphorylation Sites Encode Their Sensitivity to Starvation and Rapamycin
Seong A. Kang,Michael E. Pacold,Christopher L. Cervantes,Daniel Lim,Hua Jane Lou,Kathleen Ottina,Nathanael S. Gray,Benjamin E. Turk,Michael B. Yaffe,Michael B. Yaffe,David M. Sabatini +10 more
TL;DR: The hypothesis is that differences in substrate quality are one mechanism for allowing downstream effectors of mTORC1 to respond differentially to temporal and intensity changes in the levels of nutrients and growth factors as well as pharmacological inhibitors such as rapamycin.
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Kinome-wide Decoding of Network-Attacking Mutations Rewiring Cancer Signaling
Pau Creixell,Erwin M. Schoof,Craig D. Simpson,James Longden,Chad J. Miller,Hua Jane Lou,Lara Perryman,Thomas R. Cox,Nevena Zivanovic,Antonio Palmeri,Agata Wesolowska-Andersen,Manuela Helmer-Citterich,Jesper Ferkinghoff-Borg,Hiroaki Itamochi,Bernd Bodenmiller,Janine T. Erler,Benjamin E. Turk,Rune Linding,Rune Linding +18 more
TL;DR: Six types of network-attacking mutations (NAMs) are identified, including changes in kinase and SH2 modulation, network rewiring, and the genesis and extinction of phosphorylation sites, and mutant molecular logic gates and kinase-inactivating hotspots in cancer are discovered.
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Homing in: Mechanisms of Substrate Targeting by Protein Kinases
Chad J. Miller,Benjamin E. Turk +1 more
TL;DR: Recent progress in understanding mechanisms of kinase substrate specificity and how they function to shape cellular signaling networks is reviewed.
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Regulation of Autophagy By Signaling Through the Atg1/ULK1 Complex
Daniel Papinski,Claudine Kraft +1 more
TL;DR: The available information on both upstream regulation and downstream effectors of Atg1/ULK1, with special focus on reported and proposed kinase substrates are discussed.
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Structural and Functional Analysis of the Cdk13/Cyclin K Complex
Ann Katrin Greifenberg,Dana Hönig,Kveta Pilarova,Robert Düster,Robert Düster,Koen Bartholomeeusen,Christian A. Bösken,Christian A. Bösken,Kanchan Anand,Dalibor Blazek,Matthias Geyer,Matthias Geyer,Matthias Geyer +12 more
TL;DR: Using recombinant proteins, this work finds that flavopiridol inhibits Cdk7 more potently than it does Cdk13, and provides insights into the structure, function, and activity of human Cdk 13/CycK.
References
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The Protein Kinase Complement of the Human Genome
TL;DR: The protein kinase complement of the human genome is catalogued using public and proprietary genomic, complementary DNA, and expressed sequence tag sequences to provide a starting point for comprehensive analysis of protein phosphorylation in normal and disease states and a detailed view of the current state of human genome analysis through a focus on one large gene family.
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PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
Peter Hornbeck,Jon M. Kornhauser,Sasha Tkachev,Bin Zhang,Elzbieta Skrzypek,Beth L. Murray,Vaughan Latham,Michael Sullivan +7 more
TL;DR: PhosphoSitePlus as discussed by the authors is an open, comprehensive, manually curated and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins.
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Mechanisms of specificity in protein phosphorylation
TL;DR: A typical protein kinase must recognize between one and a few hundred bona fide phosphorylation sites in a background of ∼700,000 potentially phosphorylatable residues.
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LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1
Jose M. Lizcano,Olga Göransson,Rachel Toth,Maria Deak,Nick A. Morrice,Jérôme Boudeau,Simon A. Hawley,Lina Udd,Tomi P. Mäkelä,D. Grahame Hardie,Dario R. Alessi +10 more
TL;DR: The results show that LKB1 functions as a master upstream protein kinase, regulating AMPK‐related kinases as well as AMPK, and may mediate the physiological effects of L KB1, including its tumour suppressor function.
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Presenting your structures: the CCP4mg molecular-graphics software.
TL;DR: The CCP4 molecular-graphics program now uses the Qt framework to provide a modern look and feel and there are many new features including rendering for publication-quality images and sequence alignment.